1.13.12.7: firefly luciferase
This is an abbreviated version!
For detailed information about firefly luciferase, go to the full flat file.
Word Map on EC 1.13.12.7
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1.13.12.7
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bioluminescence
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luminescence
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chemiluminescence
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emit
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renilla
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noninvasive
-
luciferases
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cypridina
-
photon
-
lentiviral
-
adenovirus
-
click
-
luciferase-expressing
-
herpes
-
engraft
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nude
-
co-transfected
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cytomegalovirus
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camera
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electroporation
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simplex
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hsp70
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emitter
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replication-deficient
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excited-state
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promoter-driven
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charge-coupled
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nonviral
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nanoluc
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non-invasively
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gaussia
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luminol
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intramyocardial
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coelenterazine
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bicistronic
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yellow-green
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molecular biology
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light-emitting
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cap-independent
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aequorin
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biotechnology
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red-shifted
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dnaj
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luminometer
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grpe
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polyethylenimine
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bioimaging
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luciferase-based
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medicine
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photoproteins
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glow
-
analysis
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multicolor
-
brighter
- 1.13.12.7
-
bioluminescence
-
luminescence
-
chemiluminescence
-
emit
- renilla
-
noninvasive
- luciferases
- cypridina
-
photon
-
lentiviral
- adenovirus
-
click
-
luciferase-expressing
-
herpes
-
engraft
-
nude
-
co-transfected
- cytomegalovirus
-
camera
-
electroporation
- simplex
- hsp70
-
emitter
-
replication-deficient
-
excited-state
-
promoter-driven
-
charge-coupled
-
nonviral
- nanoluc
-
non-invasively
- gaussia
- luminol
-
intramyocardial
- coelenterazine
-
bicistronic
-
yellow-green
- molecular biology
-
light-emitting
-
cap-independent
- aequorin
- biotechnology
-
red-shifted
- dnaj
-
luminometer
- grpe
- polyethylenimine
-
bioimaging
-
luciferase-based
- medicine
-
photoproteins
-
glow
- analysis
-
multicolor
-
brighter
Reaction
Synonyms
AL1, AL2, beetle luciferase, CBG99luc, CBRluc, FFL, firefly luciferase, firefly luciferin luciferase, fluc, LpLuc1, LpLuc2, Luc, Luc1, Luc1-type luciferase, Luc2, Luc2-type luciferase, luciferase, luciferase (firefly luciferin), luciferase FM, luciferin, Luciola italica luciferase, lucPpe, lucPpy, orange light-producing luciferase, oxygen 4-oxidoreductase, PC3-Luc, Photinus luciferin 4-monooxygenase (ATP-hydrolyzing), Photinus pyralis luciferase, PML, PpLase, Ppy, Ppy GR-TS, Ppy RE-TS, PpyWT, PsntWT
ECTree
Advanced search results
KM Value
KM Value on EC 1.13.12.7 - firefly luciferase
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0.176
(4S)-2-(6-hydroxy-1,3-benzoxazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
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pH 8.5, temperature not specified in the publication
0.07
(4S)-2-(6-hydroxy-1-benzofuran-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
0.061
(4S)-2-(6-hydroxy-1-benzothiophen-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 9.1, temperature not specified in the publication
0.02
(4S)-2-(6-hydroxy-1H-benzimidazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
0.00025
-
pH 8.6, wild-type enzyme
0.0003
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme F250S
0.0003
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme G246A
0.0003
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, wild-type enzyme
0.0004
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme A243G
0.0008
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme S247F
0.001
ATP
mutant enzyme I423L/D436G/L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.0038
ATP
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150 microM luciferin, presence of 1 microM of N-quinolin-2-ylbenzamide, two-site binding model
0.004
ATP
free enzyme, in 0.02 M Tris-acetate buffer, pH 7.8, containing 12 mM magnesium acetate, 0.2 mM EDTA, and 0.3 mM dithiothreitol
0.004
ATP
-
pH 8.0, temperature not specified in the publication, isoenzyme AL1
0.007
ATP
-
pH 8.0, temperature not specified in the publication, isoenzyme AL2
0.008
ATP
mutant I423L/D436G/L530R, in the presence of 0.001 mM D-luciferin
0.009
ATP
mutant enzyme D436G, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.009
ATP
mutant enzyme D436G, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.029
ATP
recombinant mutant enzyme G246A, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.04
ATP
pH 7.8, temperature not specified in the publication, mutant enzyme H489M
0.041
ATP
recombinant mutant enzyme V241I/G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.0456
ATP
mutant enzyme I432L, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.047
ATP
mutant enzyme I423L, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.0538
ATP
mutant enzyme L530R, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.054
ATP
mutant enzyme L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.06
ATP
recombinant mutant enzyme G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.06
ATP
recombinant mutant enzyme G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.06
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][acetate]
0.06
ATP
pH 7.8, temperature not specified in the publication, mutant enzyme H489K
0.06
ATP
pH 7.8, temperature not specified in the publication, wild-type enzyme
0.061
ATP
recombinant mutant enzyme G246A/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.077
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][acetate]
0.0778
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][lactate]
0.0778
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][propionate]
0.09
ATP
pH 7.8, temperature not specified in the publication, mutant enzyme H489D
0.093
ATP
recombinant mutant enzyme V241I/G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.094
ATP
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150 microM luciferin, presence of 1 microM of N-quinolin-2-ylbenzamide, two-site binding model
0.0955
ATP
in 50 mM Tricine-NaOH buffer with 10 mM MgSO4, at pH 7.8
0.1
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][triflouroacetate]
0.1
ATP
pH 7.8, temperature not specified in the publication, mutant enzyme H461D
0.1 - 1
ATP
-
pH 7.8, temperature not specified in the publication, native enzyme
0.11
ATP
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two catalytically active sites: first site with a Km for ATP of 0.11 mM is responsible for initial flash, a second site with a Km for ATP of 0.02 mM catalyses the continuous low production of light
0.111
ATP
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pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][trichloroacetate]
0.111
ATP
-
pH 7.8, temperature not specified in the publication, native enzyme
0.1125
ATP
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pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][lactate]
0.133
ATP
recombinant mutant enzyme F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.151
ATP
recombinant mutant enzyme V241I/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.154
ATP
pH 7.5, temperature not specified in the publication
0.16
ATP
recombinant mutant enzyme V241I/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.16
ATP
recombinant wild type enzyme, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.16
ATP
wild type enzyme, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.1602
ATP
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.166
ATP
recombinant mutant enzyme F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.182
ATP
recombinant mutant enzyme V241I/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.215
ATP
recombinant mutant enzyme F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.283
ATP
recombinant mutant enzyme V241I, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.7
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][propionate]
1.666
ATP
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pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][triflouroacetate]
2.25
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][trichloroacetate]
83
ATP
pH and temperature not specified in the publication, wild-type enzyme
88
ATP
pH and temperature not specified in the publication, mutant enzyme L300K
100
ATP
pH and temperature not specified in the publication, mutant enzyme L300R
140
ATP
pH and temperature not specified in the publication, mutant enzyme L300E
0.002
D-firefly luciferin
pH 7.8, temperature not specified in the publication, mutant enzyme H489K
0.0023
D-firefly luciferin
pH 7.8, temperature not specified in the publication, mutant enzyme H489M
0.0025
D-firefly luciferin
pH 7.8, temperature not specified in the publication, mutant enzyme H489D
0.003
D-firefly luciferin
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pH 8.0, temperature not specified in the publication, isoenzyme AL2
0.0042
D-firefly luciferin
25°C, pH 7.8, mutant enzyme T214A/A215L/I232A/F295L/E345K/I423L/D436G/L530R
0.005
D-firefly luciferin
pH 7.8, temperature not specified in the publication, mutant enzyme H461D
0.005
D-firefly luciferin
pH 7.8, temperature not specified in the publication, wild-type enzyme
0.007
D-firefly luciferin
-
pH 8.0, temperature not specified in the publication, isoenzyme AL1
0.00881
D-firefly luciferin
25°C, pH 7.8, mutant enzyme T214A/A215L/I232A/F295L/E345K
0.015
D-firefly luciferin
pH 7.8, 22°C, recombinant mutant F255Y
0.019
D-firefly luciferin
pH 7.8, 22°C, recombinant wild-type enzyme
0.023
D-firefly luciferin
pH 7.5, temperature not specified in the publication
0.024
D-firefly luciferin
pH 7.8, 22°C, recombinant mutant R213K/T214N
10
D-firefly luciferin
pH and temperature not specified in the publication, mutant enzyme L300K
12.5
D-firefly luciferin
pH and temperature not specified in the publication, wild-type enzyme
14
D-firefly luciferin
pH and temperature not specified in the publication, mutant enzyme L300R
25
D-firefly luciferin
pH and temperature not specified in the publication, mutant enzyme L300E
0.001
wild type enzyme, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.001
D-luciferin
mutant I423L/D436G/L530R, in the presence of 0.01 mM ATP
0.0018
D-luciferin
mutant enzyme D436G, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.002
D-luciferin
mutant enzyme D436G, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.0037
D-luciferin
mutant enzyme L530R, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.004
D-luciferin
mutant enzyme I423L, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.004
D-luciferin
mutant enzyme L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.004
D-luciferin
recombinant mutant enzyme G246A, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.0043
D-luciferin
mutant enzyme I432L, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.006
D-luciferin
recombinant mutant enzyme V241I/G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.008
D-luciferin
recombinant mutant enzyme V241I, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.009
D-luciferin
recombinant mutant enzyme V241I/G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.01
D-luciferin
recombinant mutant enzyme G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.01
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][acetate]
0.01
D-luciferin
-
pH 7.8, temperature not specified in the publication, native enzyme
0.011
D-luciferin
recombinant mutant enzyme G246A/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.011
D-luciferin
recombinant mutant enzyme G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.012
D-luciferin
recombinant mutant enzyme V241I/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.0125
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][lactate]
0.014
D-luciferin
recombinant mutant enzyme F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.015
D-luciferin
recombinant wild type enzyme, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.016
D-luciferin
recombinant mutant enzyme F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.02
D-luciferin
at pH 7.8, in 50 mM Tricine-NaOH buffer with 10 mM MgSO4
0.02
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][triflouroacetate]
0.021
D-luciferin
mutant enzyme I423L/D436G/L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.0211
D-luciferin
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.022
D-luciferin
recombinant mutant enzyme F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.024
D-luciferin
recombinant mutant enzyme V241I/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.024
D-luciferin
recombinant mutant enzyme V241I/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.03
D-luciferin
at pH 7.8, in 50 mM Tricine-NaOH buffer with 10 mM MgSO4
0.0625
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][lactate]
0.07
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][trichloroacetate]
0.2
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][propionate]
0.5
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][triflouroacetate]
1
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][acetate]
1
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][propionate]
2.5
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][trichloroacetate]
0.00055
D-luciferyl-O-adenosine monophosphate
mutant enzyme K443A/K529A
0.008
Luciferin
free enzyme, in 0.02 M Tris-acetate buffer, pH 7.8, containing 12 mM magnesium acetate, 0.2 mM EDTA, and 0.3 mM dithiothreitol
0.016
Luciferin
-
90 microM ATP, presence of 0.1 microM of N-quinolin-2-ylbenzamide
0.053
Luciferin
-
90 microM ATP, presence of 1 microM of N-quinolin-2-ylbenzamide
0.0006
-
pH 8.6, mutant enzyme A243G
0.0008
luciferyl-O-adenosine monophosphate
-
pH 8.6, wild-type enzyme
0.0046
luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme S247F
additional information
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increase of the Km with increasing ionic strength
-
additional information
additional information
the Km value for the reaction intermediate D-firefly luciferin-AMP is 0.14 mM
-
additional information
additional information
-
the Km value for the reaction intermediate D-firefly luciferin-AMP is 0.14 mM
-
additional information
additional information
the Km value for the reaction intermediate D-firefly luciferin-AMP is 0.24 mM
-
additional information
additional information
-
the Km value for the reaction intermediate D-firefly luciferin-AMP is 0.24 mM
-